Adrenergic, dopaminergic, and muscarinic receptor stimulation leads to PKA phosphorylation of Na-K-ATPase.

Détails

ID Serval
serval:BIB_1ED6C06C35A9
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Adrenergic, dopaminergic, and muscarinic receptor stimulation leads to PKA phosphorylation of Na-K-ATPase.
Périodique
American Journal of Physiology
Auteur(s)
Beguin P., Beggah A., Cotecchia S., Geering K.
ISSN
0002-9513 (Print)
ISSN-L
0002-9513
Statut éditorial
Publié
Date de publication
1996
Volume
270
Numéro
1 Pt 1
Pages
C131-C137
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Résumé
Na-K-adenosinetriphosphatase (Na-K-ATPase) is a potential target for phosphorylation by protein kinase A (PKA) and C (PKC). We have investigated whether the Na-K-ATPase alpha-subunit becomes phosphorylated at its PKA or PKC phosphorylation sites upon stimulation of G protein-coupled receptors primarily linked either to the PKA or the PKC pathway. COS-7 cells, transiently or stably expressing Bufo marinus Na-K-ATPase wild-type alpha- or mutant alpha-subunits affected in its PKA or PKC phosphorylation site, were transfected with recombinant DNA encoding beta 2- or alpha 1-adrenergic (AR), dopaminergic (D1A-R), or muscarinic cholinergic (M1-AChR) receptor subspecies. Agonist stimulation of beta 2-AR or D1A-R led to phosphorylation of the wild-type alpha-subunit, as well as the PKC mutant, but not of the PKA mutant, indicating that these receptors can phosphorylate the Na-K-ATPase via PKA activation. Surprisingly, stimulation of the alpha 1B-AR, alpha 1C-AR, and M1-AChR also increased the phosphorylation of the wild-type alpha-subunit and its PKC mutant but not of its PKA mutant. Thus the phosphorylation induced by these primarily phospholipase C-linked receptors seems mainly mediated by PKA activation. These data indicate that the Na-K-ATPase alpha-subunit can act as an ultimate target for PKA phosphorylation in a cascade starting with agonist-receptor interaction and leading finally to a phosphorylation-mediated regulation of the enzyme.
Mots-clé
Animals, Bufo marinus/genetics, Cell Line, Cyclic AMP-Dependent Protein Kinases/agonists, Cyclic AMP-Dependent Protein Kinases/metabolism, Dopamine Agonists/pharmacology, Epinephrine/pharmacology, Muscarinic Agonists/pharmacology, Mutation, Phosphorylation, Protein Kinase C/genetics, Protein Kinase C/metabolism, Receptors, Adrenergic/metabolism, Receptors, Dopamine/metabolism, Receptors, Muscarinic/metabolism, Sodium-Potassium-Exchanging ATPase/genetics, Sodium-Potassium-Exchanging ATPase/metabolism, Transfection
Pubmed
Web of science
Création de la notice
24/01/2008 11:05
Dernière modification de la notice
20/08/2019 12:54
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